Endogenous targeted protein degradation in bacteria occurs in part through the tmRNA system which uses the small peptide ssrA to direct proteins to the endogenous ClpXP and ClpAP proteases for rapid degradation6,7. Biologists use variants of the E. coli ssrA tag (ec-ssrA) to modify the degradation rate of attached proteins in bacteria8 and recently in eukaryotes9, but these tags do not provide adjustable control of degradation in bacteria because the dominant ClpXP protease is constitutively expressed and cannot be easily regulated due to its integral role in many cellular processes10. Davis et al.11 used modified ec-ssrA tags and a split SspB adaptor to enable inducible degradation in this system, but the technique requires genomic disruption of the tmRNA system and is incompatible with existing genetic constructs that use ec-ssrA-mediated degradation. Recent eukaryotic degradation systems that enable small-molecule induced degradation rely on endogenous degradation machinery not present in bacteria12-14.